Ontology highlight
ABSTRACT:
SUBMITTER: Gfeller D
PROVIDER: S-EPMC1794291 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Gfeller D D De Los Rios P P Caflisch A A Rao F F
Proceedings of the National Academy of Sciences of the United States of America 20070131 6
The kinetics of biomolecular isomerization processes, such as protein folding, is governed by a free-energy surface of high dimensionality and complexity. As an alternative to projections into one or two dimensions, the free-energy surface can be mapped into a weighted network where nodes and links are configurations and direct transitions among them, respectively. In this work, the free-energy basins and barriers of the alanine dipeptide are determined quantitatively using an algorithm to parti ...[more]